P20333 (TNR1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tumor necrosis factor receptor superfamily member 1B

Alternative name(s):
Tumor necrosis factor receptor 2
Short name=TNF-R2
Tumor necrosis factor receptor type II
Short name=TNF-RII
Short name=TNFR-II
p75
p80 TNF-alpha receptor
CD_antigen=CD120b
INN=Etanercept

Cleaved into the following 2 chains:

1. Tumor necrosis factor receptor superfamily member 1b, membrane form
2. Tumor necrosis factor-binding protein 2
   Alternative name(s):
   TBP-2
   TBPII

Gene names

Name:	TNFRSF1B
Synonyms:	TNFBR, TNFR2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the metabolic effects of TNF-alpha. Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha function by antagonizing its biological activity. Ref.4 Ref.19
Subunit structure	Binds to TRAF2. Interacts with BMX. Ref.18 Ref.19
Subcellular location	Isoform 1: Cell membrane; Single-pass type I membrane protein Ref.4. Isoform 2: Secreted Ref.4. Tumor necrosis factor-binding protein 2: Secreted Ref.4.
Post-translational modification	Phosphorylated; mainly on serine residues and with a very low level on threonine residues. A soluble form (tumor necrosis factor binding protein 2) is produced from the membrane form by proteolytic processing.
Pharmaceutical use	Available under the name Enbrel (Immunex and Wyeth-Ayerst). Used to treat moderate to severe rheumatoid arthritis (RA). Enbrel consist of the extracellular ligand-binding portion of TNFRSF1B linked to an immunoglobulin Fc chain. It binds to TNF-alpha and blocks its interactions with receptors.
Sequence similarities	Contains 4 TNFR-Cys repeats.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Pharmaceutical Reference proteome
Gene Ontology (GO)
Biological_process	RNA destabilization Inferred from electronic annotation. Source: Compara apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cellular response to growth factor stimulus Inferred from electronic annotation. Source: Compara cellular response to lipopolysaccharide Inferred from mutant phenotype PubMed 22480688. Source: BHF-UCL immune response Inferred from electronic annotation. Source: Compara inflammatory response Inferred from electronic annotation. Source: Compara negative regulation of inflammatory response Inferred from electronic annotation. Source: Compara positive regulation of membrane protein ectodomain proteolysis Inferred from mutant phenotype PubMed 22480688. Source: BHF-UCL
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane raft Inferred from direct assay PubMed 17010968. Source: BHF-UCL neuronal cell body Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell varicosity Inferred from electronic annotation. Source: Compara
Molecular_function	tumor necrosis factor-activated receptor activity Traceable author statement PubMed 8702885. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P20333-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P20333-2)

Also known as: DS-TNFR2(Delta7,8); sTNFR2;

The sequence of this isoform differs from the canonical sequence as follows:
     263-268: GLIVGV → ASLACR
     269-461: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.11

Chain

23 – 461

439

Tumor necrosis factor receptor superfamily member 1b, membrane form

PRO_0000034548

Chain

27 – ?

Tumor necrosis factor-binding protein 2

PRO_0000034549

Regions

Topological domain

23 – 257

235

Extracellular Potential

Transmembrane

258 – 287

30

Helical; Potential

Topological domain

288 – 461

174

Cytoplasmic Potential

Repeat

39 – 76

38

TNFR-Cys 1

Repeat

77 – 118

42

TNFR-Cys 2

Repeat

119 – 162

44

TNFR-Cys 3

Repeat

163 – 201

39

TNFR-Cys 4

Amino acid modifications

Glycosylation

171

1

N-linked (GlcNAc...) Potential

Glycosylation

193

1

N-linked (GlcNAc...) Potential

Disulfide bond

40 ↔ 53

By similarity

Disulfide bond

54 ↔ 67

By similarity

Disulfide bond

57 ↔ 75

By similarity

Disulfide bond

78 ↔ 93

By similarity

Disulfide bond

96 ↔ 110

By similarity

Disulfide bond

100 ↔ 118

By similarity

Disulfide bond

120 ↔ 126

By similarity

Disulfide bond

134 ↔ 143

By similarity

Disulfide bond

137 ↔ 161

By similarity

Disulfide bond

164 ↔ 179

By similarity

Natural variations

Alternative sequence

263 – 268

6

GLIVGV → ASLACR in isoform 2.

VSP_011826

Alternative sequence

269 – 461

193

Missing in isoform 2.

VSP_011827

Natural variant

187

1

V → M. Ref.6
Corresponds to variant rs2228494 [ dbSNP | Ensembl ].

VAR_017176

Natural variant

196

1

M → R Frequent polymorphism; seems to be associated with hyperandrogenism, polycystic ovary syndrome (PCOS) and systemic lupus erythematosus. Ref.1 Ref.6 Ref.7 Ref.15 Ref.16 Ref.21 Ref.22
Corresponds to variant rs1061622 [ dbSNP | Ensembl ].

VAR_015434

Natural variant

232

1

E → K. Ref.6 Ref.7 Ref.16 Ref.21
Corresponds to variant rs5746026 [ dbSNP | Ensembl ].

VAR_015435

Natural variant

236

1

A → T. Ref.6
Corresponds to variant rs5746027 [ dbSNP | Ensembl ].

VAR_017177

Natural variant

264

1

L → P. Ref.6
Corresponds to variant rs2229700 [ dbSNP | Ensembl ].

VAR_017178

Natural variant

269

1

T → P. Ref.7
Corresponds to variant rs17879042 [ dbSNP | Ensembl ].

VAR_017179

Natural variant

295

1

Q → R. Ref.6
Corresponds to variant rs5746032 [ dbSNP | Ensembl ].

VAR_017180

Natural variant

301

1

P → R. Ref.7
Corresponds to variant rs17883432 [ dbSNP | Ensembl ].

VAR_017181

Experimental info

Sequence conflict

35 – 37

3

EPG → APT AA sequence Ref.12

Sequence conflict

98

1

S → P in AAN72434. Ref.4

Sequence conflict

102

1

S → P in AAN72434. Ref.4

Sequence conflict

141

1

R → P in AAA63262. Ref.15

Sequence conflict

363

1

A → T in AAA63262. Ref.15

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

461

Helix Strand Turn

Details...

Beta strand

44 – 47

4

Turn

48 – 51

4

Beta strand

52 – 55

4

Beta strand

61 – 65

5

Beta strand

74 – 77

4

Beta strand

86 – 88

3

Beta strand

104 – 108

5

Beta strand

112 – 114

3

Beta strand

117 – 120

4

Beta strand

124 – 129

6

Beta strand

131 – 139

9

Beta strand

147 – 151

5

Turn

154 – 156

3

Beta strand

160 – 163

4

Beta strand

174 – 176

3

Beta strand

194 – 196

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 27, 2002. Version 3. Checksum: 603D0AE1CD69ACBF	FASTA	461	48,291
	10 20 30 40 50 60 MAPVAVWAAL AVGLELWAAA HALPAQVAFT PYAPEPGSTC RLREYYDQTA QMCCSKCSPG 70 80 90 100 110 120 QHAKVFCTKT SDTVCDSCED STYTQLWNWV PECLSCGSRC SSDQVETQAC TREQNRICTC 130 140 150 160 170 180 RPGWYCALSK QEGCRLCAPL RKCRPGFGVA RPGTETSDVV CKPCAPGTFS NTTSSTDICR 190 200 210 220 230 240 PHQICNVVAI PGNASMDAVC TSTSPTRSMA PGAVHLPQPV STRSQHTQPT PEPSTAPSTS 250 260 270 280 290 300 FLLPMGPSPP AEGSTGDFAL PVGLIVGVTA LGLLIIGVVN CVIMTQVKKK PLCLQREAKV 310 320 330 340 350 360 PHLPADKARG TQGPEQQHLL ITAPSSSSSS LESSASALDR RAPTRNQPQA PGVEASGAGE 370 380 390 400 410 420 ARASTGSSDS SPGGHGTQVN VTCIVNVCSS SDHSSQCSSQ ASSTMGDTDS SPSESPKDEQ 430 440 450 460 VPFSKEECAF RSQLETPETL LGSTEEKPLP LGVPDAGMKP S
	Isoform 2 (DS-TNFR2(Delta7,8)) (sTNFR2) [UniParc]. Checksum: 51A97BA5222FA444	FASTA	268	28,461
	10 20 30 40 50 60 MAPVAVWAAL AVGLELWAAA HALPAQVAFT PYAPEPGSTC RLREYYDQTA QMCCSKCSPG 70 80 90 100 110 120 QHAKVFCTKT SDTVCDSCED STYTQLWNWV PECLSCGSRC SSDQVETQAC TREQNRICTC 130 140 150 160 170 180 RPGWYCALSK QEGCRLCAPL RKCRPGFGVA RPGTETSDVV CKPCAPGTFS NTTSSTDICR 190 200 210 220 230 240 PHQICNVVAI PGNASMDAVC TSTSPTRSMA PGAVHLPQPV STRSQHTQPT PEPSTAPSTS 250 260 FLLPMGPSPP AEGSTGDFAL PVASLACR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A second tumor necrosis factor receptor gene product can shed a naturally occurring tumor necrosis factor inhibitor." Kohno T., Brewer M.T., Baker S.L., Schwartz P.E., King M.W., Hale K.K., Squires C.H., Thompson R.C., Vannice J.L. Proc. Natl. Acad. Sci. U.S.A. 87:8331-8335(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-196.
[2]	"A receptor for tumor necrosis factor defines an unusual family of cellular and viral proteins." Smith C.A., Davis T., Anderson D., Solam L., Beckmann M.P., Jerzy R., Dower S.K., Cosman D., Goodwin R.G. Science 248:1019-1023(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Physical mapping and genomic structure of the human TNFR2 gene." Beltinger C.P., White P.S., Maris J.M., Sulman E.P., Jensen S.J., Lepaslier D., Stallard B.J., Goeddel D.V., Desauvage F.J., Brodeur G.M. Genomics 35:94-100(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]	"Identification and characterization of a novel spliced variant that encodes human soluble tumor necrosis factor receptor 2." Lainez B., Fernandez-Real J.M., Romero X., Esplugues E., Canete J.D., Ricart W., Engel P. Int. Immunol. 16:169-177(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, FUNCTION (ISOFORM 2).
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	NIEHS SNPs program Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-187; ARG-196; LYS-232; THR-236; PRO-264 AND ARG-295.
[7]	SeattleSNPs variation discovery resource Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-196; LYS-232; PRO-269 AND ARG-301.
[8]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: PNS.
[11]	"Purification and partial amino acid sequence analysis of two distinct tumor necrosis factor receptors from HL60 cells." Loetscher H., Schlaeger E.J., Lahm H.-W., Pan Y.-C.E., Lesslauer W., Brockhaus M. J. Biol. Chem. 265:20131-20138(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-40; 65-69; 136-141; 300-306 AND 346-362.
[12]	"Purification of two types of TNF inhibitors in the urine of the patient with chronic glomerulonephritis." Suzuki J., Tomizawa S., Arai H., Seki Y., Maruyama K., Kuroume T. Nephron 66:386-390(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-37. Tissue: Urine.
[13]	"Two tumor necrosis factor-binding proteins purified from human urine. Evidence for immunological cross-reactivity with cell surface tumor necrosis factor receptors." Engelmann H., Novick D., Wallach D. J. Biol. Chem. 265:1531-1536(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-31. Tissue: Urine.
[14]	"Two human TNF receptors have similar extracellular, but distinct intracellular, domain sequences." Dembic Z., Loetscher H., Gubler U., Pan Y.C., Lahm H.-W., Gentz R., Brockhaus M., Lesslauer W. Cytokine 2:231-237(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-461 (ISOFORM 1).
[15]	"Complementary DNA cloning of a receptor for tumor necrosis factor and demonstration of a shed form of the receptor." Heller R.A., Song K., Onasch M.A., Fischer W.H., Chang D., Ringold G.M. Proc. Natl. Acad. Sci. U.S.A. 87:6151-6155(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 116-461 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT ARG-196.
[16]	"New single nucleotide polymorphisms in the coding region of human TNFR2: association with systemic lupus erythematosus." Tsuchiya N., Komata T., Matsushita M., Ohashi J., Tokunaga K. Genes Immun. 1:501-503(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 154-183, VARIANTS ARG-196 AND LYS-232.
[17]	"Biochemical properties of the 75-kDa tumor necrosis factor receptor. Characterization of ligand binding, internalization, and receptor phosphorylation." Pennica D., Lam V.T., Mize N.K., Weber R.F., Lewis M., Fendly B.M., Lipari M.T., Goeddel D.V. J. Biol. Chem. 267:21172-21178(1992) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[18]	"A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor." Rothe M., Wong S.C., Henzel W.J., Goeddel D.V. Cell 78:681-692(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRAF2.
[19]	"Etk/Bmx as a tumor necrosis factor receptor type 2-specific kinase: role in endothelial cell migration and angiogenesis." Pan S., An P., Zhang R., He X., Yin G., Min W. Mol. Cell. Biol. 22:7512-7523(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH BMX.
[20]	"Structural basis for self-association and receptor recognition of human TRAF2." Park Y.C., Burkitt V., Villa A.R., Tong L., Wu H. Nature 398:533-538(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 419-428 IN COMPLEX WITH TRAF2.
[21]	"Association of tumor necrosis factor receptor type II polymorphism 196R with systemic lupus erythematosus in the Japanese: molecular and functional analysis." Morita C., Horiuchi T., Tsukamoto H., Hatta N., Kikuchi Y., Arinobu Y., Otsuka T., Sawabe T., Harashima S., Nagasawa K., Niho Y. Arthritis Rheum. 44:2819-2827(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ARG-196 AND LYS-232.
[22]	"Comment: the methionine 196 arginine polymorphism in exon 6 of the TNF receptor 2 gene (TNFRSF1B) is associated with the polycystic ovary syndrome and hyperandrogenism." Peral B., San Millan J.L., Castello R., Moghetti P., Escobar-Morreale H.F. J. Clin. Endocrinol. Metab. 87:3977-3983(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ARG-196.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

NIEHS-SNPs

Enbrel

Clinical information on Enbrel

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M55994 mRNA. Translation: AAA36755.1.
M32315 mRNA. Translation: AAA59929.1.
U52165 , U52156, U52157, U52158, U52159, U52160, U52161, U52162, U52163, U52164 Genomic DNA. Translation: AAC50622.1.
AY148473 mRNA. Translation: AAN72434.1.
BT019927 mRNA. Translation: AAV38730.1.
AY264804 Genomic DNA. Translation: AAO89076.1.
AY342040 Genomic DNA. Translation: AAP88939.1.
AL031276, AL357835 Genomic DNA. Translation: CAI19225.1.
AL357835, AL031276 Genomic DNA. Translation: CAH73721.1.
CH471130 Genomic DNA. Translation: EAW71733.1.
BC052977 mRNA. Translation: AAH52977.1.
S63368 mRNA. Translation: AAB19824.2.
M35857 mRNA. Translation: AAA63262.1.
AB030950 Genomic DNA. Translation: BAA89053.1.

IPI

IPI00023501.
IPI00473089.

PIR

A35356.

RefSeq

NP_001057.1. NM_001066.2.

UniGene

Hs.256278.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CA9	X-ray	2.30	G/H	420-428	[»]
3ALQ	X-ray	3.00	R/S/T/U/V/W	33-205	[»]

ProteinModelPortal

P20333.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-78N.

IntAct

P20333. 9 interactions.

MINT

MINT-134958.

STRING

9606.ENSP00000365435.

PTM databases

PhosphoSite

P20333.

Polymorphism databases

DMDM

21264534.

Proteomic databases

PaxDb

P20333.

PeptideAtlas

P20333.

PRIDE

P20333.

Protocols and materials databases

DNASU

7133.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000376259; ENSP00000365435; ENSG00000028137.

GeneID

7133.

KEGG

hsa:7133.

UCSC

uc001att.3. human.

Organism-specific databases

CTD

7133.

GeneCards

GC01P012161.

HGNC

HGNC:11917. TNFRSF1B.

HPA

CAB013045.
HPA004796.

MIM

191191. gene.

neXtProt

NX_P20333.

PharmGKB

PA36610.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG42764.

HOGENOM

HOG000132845.

HOVERGEN

HBG054237.

InParanoid

P20333.

KO

K05141.

OMA

KDEQVPF.

OrthoDB

EOG48D0W0.

PhylomeDB

P20333.

Enzyme and pathway databases

Pathway_Interaction_DB

tnfpathway. TNF receptor signaling pathway.

Gene expression databases

ArrayExpress

P20333.

Bgee

P20333.

CleanEx

HS_TNFRSF1B.

Genevestigator

P20333.

GermOnline

ENSG00000028137. Homo sapiens.

Family and domain databases

InterPro

IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR020411. TNFR_1B.
[Graphical view]

Pfam

PF00020. TNFR_c6. 2 hits.
[Graphical view]

PRINTS

PR01919. TNFACTORR1B.

SMART

SM00208. TNFR. 4 hits.
[Graphical view]

PROSITE

PS00652. TNFR_NGFR_1. 2 hits.
PS50050. TNFR_NGFR_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1250356.

DrugBank

DB00005. Etanercept.
DB00065. Infliximab.

EvolutionaryTrace

P20333.

GenomeRNAi

7133.

NextBio

27909.

PMAP-CutDB

P20333.

SOURCE

Search...

Entry information

Entry name

TNR1B_HUMAN

Accession

Primary (citable) accession number: P20333
Secondary accession number(s): B1AJZ3 , Q16042, Q6YI29, Q9UIH1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	May 27, 2002
Last modified:	May 1, 2013
This is version 157 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.